#ID(s) interactor A	ID(s) interactor B	Alt. ID(s) interactor A	Alt. ID(s) interactor B	Alias(es) interactor A	Alias(es) interactor B	Interaction detection method(s)	Publication 1st author(s)	Publication Identifier(s)	Taxid interactor A	Taxid interactor B	Interaction type(s)	Source database(s)	Interaction identifier(s)	Confidence value(s)	Expansion method(s)	Biological role(s) interactor A	Biological role(s) interactor B	Experimental role(s) interactor A	Experimental role(s) interactor B	Type(s) interactor A	Type(s) interactor B	Xref(s) interactor A	Xref(s) interactor B	Interaction Xref(s)	Annotation(s) interactor A	Annotation(s) interactor B	Interaction annotation(s)	Host organism(s)	Interaction parameter(s)	Creation date	Update date	Checksum(s) interactor A	Checksum(s) interactor B	Interaction Checksum(s)	Negative	Feature(s) interactor A	Feature(s) interactor B	Stoichiometry(s) interactor A	Stoichiometry(s) interactor B	Identification method participant A	Identification method participant B
uniprotkb:Q9H9S5	uniprotkb:Q9H9S5	intact:EBI-21505709|ensembl:ENSP00000326570|ensembl:ENSP00000375776|uniprotkb:A8K5G7	intact:EBI-21505709|ensembl:ENSP00000326570|ensembl:ENSP00000375776|uniprotkb:A8K5G7	psi-mi:fkrp_human(display_long)|uniprotkb:Ribitol-5-phosphate transferase(gene name synonym)|uniprotkb:FKRP(gene name)|psi-mi:FKRP(display_short)	psi-mi:fkrp_human(display_long)|uniprotkb:Ribitol-5-phosphate transferase(gene name synonym)|uniprotkb:FKRP(gene name)|psi-mi:FKRP(display_short)	psi-mi:"MI:0114"(x-ray crystallography)	Kuwabara et al. (2020)	pubmed:31949166|imex:IM-28494	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-26444960|imex:IM-28494-1|wwpdb:6KAK|wwpdb:6KAN|wwpdb:6L7S|wwpdb:6L7T|wwpdb:6L7U	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	ensembl:ENSG00000181027(gene)|ensembl:ENST00000318584(transcript)|ensembl:ENST00000391909(transcript)|go:"GO:0000139"(Golgi membrane)|go:"GO:0002162"(dystroglycan binding)|go:"GO:0005615"(extracellular space)|go:"GO:0005654"(nucleoplasm)|go:"GO:0005791"(rough endoplasmic reticulum)|go:"GO:0005794"(Golgi apparatus)|go:"GO:0005829"(cytosol)|go:"GO:0016021"(integral component of membrane)|go:"GO:0016485"(protein processing)|go:"GO:0016740"(transferase activity)|go:"GO:0035269"(protein O-linked mannosylation)|go:"GO:0042383"(sarcolemma)|go:"GO:0042802"(identical protein binding)|interpro:IPR007074(LicD protein)|mint:Q9H9S5|rcsb pdb:6KAJ|rcsb pdb:6KAK|rcsb pdb:6KAL|rcsb pdb:6KAM|rcsb pdb:6KAN|rcsb pdb:6L7S|rcsb pdb:6L7T|rcsb pdb:6L7U|refseq:NP_001034974.1|refseq:NP_077277.1|refseq:XP_005259304.1|refseq:XP_005259305.1|refseq:XP_005259306.1|refseq:XP_011525608.1|refseq:XP_011525609.1|refseq:XP_016882786.1	ensembl:ENSG00000181027(gene)|ensembl:ENST00000318584(transcript)|ensembl:ENST00000391909(transcript)|go:"GO:0000139"(Golgi membrane)|go:"GO:0002162"(dystroglycan binding)|go:"GO:0005615"(extracellular space)|go:"GO:0005654"(nucleoplasm)|go:"GO:0005791"(rough endoplasmic reticulum)|go:"GO:0005794"(Golgi apparatus)|go:"GO:0005829"(cytosol)|go:"GO:0016021"(integral component of membrane)|go:"GO:0016485"(protein processing)|go:"GO:0016740"(transferase activity)|go:"GO:0035269"(protein O-linked mannosylation)|go:"GO:0042383"(sarcolemma)|go:"GO:0042802"(identical protein binding)|interpro:IPR007074(LicD protein)|mint:Q9H9S5|rcsb pdb:6KAJ|rcsb pdb:6KAK|rcsb pdb:6KAL|rcsb pdb:6KAM|rcsb pdb:6KAN|rcsb pdb:6L7S|rcsb pdb:6L7T|rcsb pdb:6L7U|refseq:NP_001034974.1|refseq:NP_077277.1|refseq:XP_005259304.1|refseq:XP_005259305.1|refseq:XP_005259306.1|refseq:XP_011525608.1|refseq:XP_011525609.1|refseq:XP_016882786.1	-	-	-	figure legend:Fig. 1, Table S1|comment:"Initially, we determined the crystal structure of human FKRP without substrates. A soluble form of FKRP (sFKRP: residues 45 to C-terminus of FKRP, 451 amino acid residues in total) was purified and crystallized, and the X-ray structures of the Mg2+ and Ba2+-bound forms were determined (see Methods and Supplementary Table 1). The asymmetrical unit contains four sFKRP subunits, which are designated as subunits (or chains) A, B, C, and D (Fig. 1a). Buried surface areas calculated by ePISA27 (Supplementary Table 2) suggested that the four sFKRP subunits form a homo-tetramer."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:9606(human-293s)|taxid:9606(Human 293S cell line)	-	2020/11/11	2020/11/13	rogid:s+HbseVnOLubWt0t2LFelTTGEvQ9606	rogid:s+HbseVnOLubWt0t2LFelTTGEvQ9606	rigid:iX7Kvig2hsKnYw6w684FHwM/CbM	false	sufficient binding region:45-495	sufficient binding region:45-495	4	0	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
chebi:"CHEBI:16022"	uniprotkb:Q9H9S5	intact:EBI-26447096|chebi:"CHEBI:13272"|chebi:"CHEBI:3273"|chebi:"CHEBI:20872"	intact:EBI-21505709|ensembl:ENSP00000326570|ensembl:ENSP00000375776|uniprotkb:A8K5G7	psi-mi:cdp-ribitol(display_short)|psi-mi:"CHEBI:16022"(display_long)|intact:CDP 5-ester with D-ribitol(synonym)|intact:Cdp ribitol(synonym)|intact:CDP-L-ribitol(synonym)|intact:CDPribitol(synonym)|intact:"Cytidine 5'-(trihydrogen diphosphate), P'-5-ester with D-ribitol"(synonym)|intact:Cytidine diphosphate ribitol(synonym)|intact:"cytidine 5'-{3-[(2R,3S,4S)-2,3,4,5-tetrahydroxypentyl] dihydrogen diphosphate}"(iupac name)	psi-mi:fkrp_human(display_long)|uniprotkb:Ribitol-5-phosphate transferase(gene name synonym)|uniprotkb:FKRP(gene name)|psi-mi:FKRP(display_short)	psi-mi:"MI:0114"(x-ray crystallography)	Kuwabara et al. (2020)	pubmed:31949166|imex:IM-28494	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-26447075|wwpdb:6kaj|imex:IM-28494-7	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0328"(small molecule)	psi-mi:"MI:0326"(protein)	-	ensembl:ENSG00000181027(gene)|ensembl:ENST00000318584(transcript)|ensembl:ENST00000391909(transcript)|go:"GO:0000139"(Golgi membrane)|go:"GO:0002162"(dystroglycan binding)|go:"GO:0005615"(extracellular space)|go:"GO:0005654"(nucleoplasm)|go:"GO:0005791"(rough endoplasmic reticulum)|go:"GO:0005794"(Golgi apparatus)|go:"GO:0005829"(cytosol)|go:"GO:0016021"(integral component of membrane)|go:"GO:0016485"(protein processing)|go:"GO:0016740"(transferase activity)|go:"GO:0035269"(protein O-linked mannosylation)|go:"GO:0042383"(sarcolemma)|go:"GO:0042802"(identical protein binding)|interpro:IPR007074(LicD protein)|mint:Q9H9S5|rcsb pdb:6KAJ|rcsb pdb:6KAK|rcsb pdb:6KAL|rcsb pdb:6KAM|rcsb pdb:6KAN|rcsb pdb:6L7S|rcsb pdb:6L7T|rcsb pdb:6L7U|refseq:NP_001034974.1|refseq:NP_077277.1|refseq:XP_005259304.1|refseq:XP_005259305.1|refseq:XP_005259306.1|refseq:XP_011525608.1|refseq:XP_011525609.1|refseq:XP_016882786.1	-	-	-	figure legend:Fig. 1, Table S1|comment:"Initially, we determined the crystal structure of human FKRP without substrates. A soluble form of FKRP (sFKRP: residues 45 to C-terminus of FKRP, 451 amino acid residues in total) was purified and crystallized, and the X-ray structures of the Mg2+ and Ba2+-bound forms were determined (see Methods and Supplementary Table 1). The asymmetrical unit contains four sFKRP subunits, which are designated as subunits (or chains) A, B, C, and D (Fig. 1a). Buried surface areas calculated by ePISA27 (Supplementary Table 2) suggested that the four sFKRP subunits form a homo-tetramer."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:9606(human-293s)|taxid:9606(Human 293S cell line)	-	2020/11/11	2020/11/13	-	rogid:s+HbseVnOLubWt0t2LFelTTGEvQ9606	-	false	-	sufficient binding region:45-495	-	4	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
chebi:"CHEBI:16022"	uniprotkb:Q9H9S5	intact:EBI-26447096|chebi:"CHEBI:13272"|chebi:"CHEBI:3273"|chebi:"CHEBI:20872"	intact:EBI-21505709|ensembl:ENSP00000326570|ensembl:ENSP00000375776|uniprotkb:A8K5G7	psi-mi:cdp-ribitol(display_short)|psi-mi:"CHEBI:16022"(display_long)|intact:CDP 5-ester with D-ribitol(synonym)|intact:Cdp ribitol(synonym)|intact:CDP-L-ribitol(synonym)|intact:CDPribitol(synonym)|intact:"Cytidine 5'-(trihydrogen diphosphate), P'-5-ester with D-ribitol"(synonym)|intact:Cytidine diphosphate ribitol(synonym)|intact:"cytidine 5'-{3-[(2R,3S,4S)-2,3,4,5-tetrahydroxypentyl] dihydrogen diphosphate}"(iupac name)	psi-mi:fkrp_human(display_long)|uniprotkb:Ribitol-5-phosphate transferase(gene name synonym)|uniprotkb:FKRP(gene name)|psi-mi:FKRP(display_short)	psi-mi:"MI:0114"(x-ray crystallography)	Kuwabara et al. (2020)	pubmed:31949166|imex:IM-28494	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-26447082|wwpdb:6kam|imex:IM-28494-9	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0328"(small molecule)	psi-mi:"MI:0326"(protein)	-	ensembl:ENSG00000181027(gene)|ensembl:ENST00000318584(transcript)|ensembl:ENST00000391909(transcript)|go:"GO:0000139"(Golgi membrane)|go:"GO:0002162"(dystroglycan binding)|go:"GO:0005615"(extracellular space)|go:"GO:0005654"(nucleoplasm)|go:"GO:0005791"(rough endoplasmic reticulum)|go:"GO:0005794"(Golgi apparatus)|go:"GO:0005829"(cytosol)|go:"GO:0016021"(integral component of membrane)|go:"GO:0016485"(protein processing)|go:"GO:0016740"(transferase activity)|go:"GO:0035269"(protein O-linked mannosylation)|go:"GO:0042383"(sarcolemma)|go:"GO:0042802"(identical protein binding)|interpro:IPR007074(LicD protein)|mint:Q9H9S5|rcsb pdb:6KAJ|rcsb pdb:6KAK|rcsb pdb:6KAL|rcsb pdb:6KAM|rcsb pdb:6KAN|rcsb pdb:6L7S|rcsb pdb:6L7T|rcsb pdb:6L7U|refseq:NP_001034974.1|refseq:NP_077277.1|refseq:XP_005259304.1|refseq:XP_005259305.1|refseq:XP_005259306.1|refseq:XP_011525608.1|refseq:XP_011525609.1|refseq:XP_016882786.1	-	-	-	figure legend:Fig. 1, Table S1|comment:"Initially, we determined the crystal structure of human FKRP without substrates. A soluble form of FKRP (sFKRP: residues 45 to C-terminus of FKRP, 451 amino acid residues in total) was purified and crystallized, and the X-ray structures of the Mg2+ and Ba2+-bound forms were determined (see Methods and Supplementary Table 1). The asymmetrical unit contains four sFKRP subunits, which are designated as subunits (or chains) A, B, C, and D (Fig. 1a). Buried surface areas calculated by ePISA27 (Supplementary Table 2) suggested that the four sFKRP subunits form a homo-tetramer."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:9606(human-293s)|taxid:9606(Human 293S cell line)	-	2020/11/11	2020/11/13	-	rogid:s+HbseVnOLubWt0t2LFelTTGEvQ9606	-	false	-	sufficient binding region:45-495	-	4	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
chebi:"CHEBI:16022"	chebi:"CHEBI:166860"	intact:EBI-26447096|chebi:"CHEBI:13272"|chebi:"CHEBI:3273"|chebi:"CHEBI:20872"	intact:EBI-26447136	psi-mi:cdp-ribitol(display_short)|psi-mi:"CHEBI:16022"(display_long)|intact:CDP 5-ester with D-ribitol(synonym)|intact:Cdp ribitol(synonym)|intact:CDP-L-ribitol(synonym)|intact:CDPribitol(synonym)|intact:"Cytidine 5'-(trihydrogen diphosphate), P'-5-ester with D-ribitol"(synonym)|intact:Cytidine diphosphate ribitol(synonym)|intact:"cytidine 5'-{3-[(2R,3S,4S)-2,3,4,5-tetrahydroxypentyl] dihydrogen diphosphate}"(iupac name)	psi-mi:m3 acceptor complex(display_short)|psi-mi:"CHEBI:166860"(display_long)	psi-mi:"MI:0114"(x-ray crystallography)	Kuwabara et al. (2020)	pubmed:31949166|imex:IM-28494	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-26447082|wwpdb:6kam|imex:IM-28494-9	-	psi-mi:"MI:1060"(spoke expansion)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0328"(small molecule)	psi-mi:"MI:0328"(small molecule)	-	-	-	-	-	figure legend:Fig. 1, Table S1|comment:"Initially, we determined the crystal structure of human FKRP without substrates. A soluble form of FKRP (sFKRP: residues 45 to C-terminus of FKRP, 451 amino acid residues in total) was purified and crystallized, and the X-ray structures of the Mg2+ and Ba2+-bound forms were determined (see Methods and Supplementary Table 1). The asymmetrical unit contains four sFKRP subunits, which are designated as subunits (or chains) A, B, C, and D (Fig. 1a). Buried surface areas calculated by ePISA27 (Supplementary Table 2) suggested that the four sFKRP subunits form a homo-tetramer."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:9606(human-293s)|taxid:9606(Human 293S cell line)	-	2020/11/11	2020/11/13	-	-	-	false	-	-	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
chebi:"CHEBI:17361"	uniprotkb:Q9H9S5	intact:EBI-26447112|chebi:"CHEBI:41312"|chebi:"CHEBI:41319"|chebi:"CHEBI:41691"|chebi:"CHEBI:41666"|chebi:"CHEBI:47362"|chebi:"CHEBI:48799"|chebi:"CHEBI:3275"|chebi:"CHEBI:13274"|chebi:"CHEBI:23520"	intact:EBI-21505709|ensembl:ENSP00000326570|ensembl:ENSP00000375776|uniprotkb:A8K5G7	psi-mi:cytidine 5'-monophosphate(display_short)|psi-mi:"CHEBI:17361"(display_long)|intact:CMP(synonym)|intact:cytidine 5'-monophosphate(synonym)|intact:Cytidine-5'-monophosphate(synonym)|intact:cytidylate(synonym)|intact:Cytidylic acid(synonym)|intact:pC(synonym)|intact:5'-cytidylic acid(iupac name)	psi-mi:fkrp_human(display_long)|uniprotkb:Ribitol-5-phosphate transferase(gene name synonym)|uniprotkb:FKRP(gene name)|psi-mi:FKRP(display_short)	psi-mi:"MI:0114"(x-ray crystallography)	Kuwabara et al. (2020)	pubmed:31949166|imex:IM-28494	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-26447089|wwpdb:6kal|imex:IM-28494-11	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0328"(small molecule)	psi-mi:"MI:0326"(protein)	-	ensembl:ENSG00000181027(gene)|ensembl:ENST00000318584(transcript)|ensembl:ENST00000391909(transcript)|go:"GO:0000139"(Golgi membrane)|go:"GO:0002162"(dystroglycan binding)|go:"GO:0005615"(extracellular space)|go:"GO:0005654"(nucleoplasm)|go:"GO:0005791"(rough endoplasmic reticulum)|go:"GO:0005794"(Golgi apparatus)|go:"GO:0005829"(cytosol)|go:"GO:0016021"(integral component of membrane)|go:"GO:0016485"(protein processing)|go:"GO:0016740"(transferase activity)|go:"GO:0035269"(protein O-linked mannosylation)|go:"GO:0042383"(sarcolemma)|go:"GO:0042802"(identical protein binding)|interpro:IPR007074(LicD protein)|mint:Q9H9S5|rcsb pdb:6KAJ|rcsb pdb:6KAK|rcsb pdb:6KAL|rcsb pdb:6KAM|rcsb pdb:6KAN|rcsb pdb:6L7S|rcsb pdb:6L7T|rcsb pdb:6L7U|refseq:NP_001034974.1|refseq:NP_077277.1|refseq:XP_005259304.1|refseq:XP_005259305.1|refseq:XP_005259306.1|refseq:XP_011525608.1|refseq:XP_011525609.1|refseq:XP_016882786.1	-	-	-	figure legend:Fig. 1, Table S1|comment:"Initially, we determined the crystal structure of human FKRP without substrates. A soluble form of FKRP (sFKRP: residues 45 to C-terminus of FKRP, 451 amino acid residues in total) was purified and crystallized, and the X-ray structures of the Mg2+ and Ba2+-bound forms were determined (see Methods and Supplementary Table 1). The asymmetrical unit contains four sFKRP subunits, which are designated as subunits (or chains) A, B, C, and D (Fig. 1a). Buried surface areas calculated by ePISA27 (Supplementary Table 2) suggested that the four sFKRP subunits form a homo-tetramer."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:9606(human-293s)|taxid:9606(Human 293S cell line)	-	2020/11/11	2020/11/13	-	rogid:s+HbseVnOLubWt0t2LFelTTGEvQ9606	-	false	-	sufficient binding region:45-495	-	4	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:Q9H9S5	uniprotkb:Q9H9S5	intact:EBI-21505709|ensembl:ENSP00000326570|ensembl:ENSP00000375776|uniprotkb:A8K5G7	intact:EBI-21505709|ensembl:ENSP00000326570|ensembl:ENSP00000375776|uniprotkb:A8K5G7	psi-mi:fkrp_human(display_long)|uniprotkb:Ribitol-5-phosphate transferase(gene name synonym)|uniprotkb:FKRP(gene name)|psi-mi:FKRP(display_short)	psi-mi:fkrp_human(display_long)|uniprotkb:Ribitol-5-phosphate transferase(gene name synonym)|uniprotkb:FKRP(gene name)|psi-mi:FKRP(display_short)	psi-mi:"MI:0826"(x ray scattering)	Kuwabara et al. (2020)	pubmed:31949166|imex:IM-28494	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-26444981|imex:IM-28494-3	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	ensembl:ENSG00000181027(gene)|ensembl:ENST00000318584(transcript)|ensembl:ENST00000391909(transcript)|go:"GO:0000139"(Golgi membrane)|go:"GO:0002162"(dystroglycan binding)|go:"GO:0005615"(extracellular space)|go:"GO:0005654"(nucleoplasm)|go:"GO:0005791"(rough endoplasmic reticulum)|go:"GO:0005794"(Golgi apparatus)|go:"GO:0005829"(cytosol)|go:"GO:0016021"(integral component of membrane)|go:"GO:0016485"(protein processing)|go:"GO:0016740"(transferase activity)|go:"GO:0035269"(protein O-linked mannosylation)|go:"GO:0042383"(sarcolemma)|go:"GO:0042802"(identical protein binding)|interpro:IPR007074(LicD protein)|mint:Q9H9S5|rcsb pdb:6KAJ|rcsb pdb:6KAK|rcsb pdb:6KAL|rcsb pdb:6KAM|rcsb pdb:6KAN|rcsb pdb:6L7S|rcsb pdb:6L7T|rcsb pdb:6L7U|refseq:NP_001034974.1|refseq:NP_077277.1|refseq:XP_005259304.1|refseq:XP_005259305.1|refseq:XP_005259306.1|refseq:XP_011525608.1|refseq:XP_011525609.1|refseq:XP_016882786.1	ensembl:ENSG00000181027(gene)|ensembl:ENST00000318584(transcript)|ensembl:ENST00000391909(transcript)|go:"GO:0000139"(Golgi membrane)|go:"GO:0002162"(dystroglycan binding)|go:"GO:0005615"(extracellular space)|go:"GO:0005654"(nucleoplasm)|go:"GO:0005791"(rough endoplasmic reticulum)|go:"GO:0005794"(Golgi apparatus)|go:"GO:0005829"(cytosol)|go:"GO:0016021"(integral component of membrane)|go:"GO:0016485"(protein processing)|go:"GO:0016740"(transferase activity)|go:"GO:0035269"(protein O-linked mannosylation)|go:"GO:0042383"(sarcolemma)|go:"GO:0042802"(identical protein binding)|interpro:IPR007074(LicD protein)|mint:Q9H9S5|rcsb pdb:6KAJ|rcsb pdb:6KAK|rcsb pdb:6KAL|rcsb pdb:6KAM|rcsb pdb:6KAN|rcsb pdb:6L7S|rcsb pdb:6L7T|rcsb pdb:6L7U|refseq:NP_001034974.1|refseq:NP_077277.1|refseq:XP_005259304.1|refseq:XP_005259305.1|refseq:XP_005259306.1|refseq:XP_011525608.1|refseq:XP_011525609.1|refseq:XP_016882786.1	-	-	-	figure legend:Fig. 2A-B|comment:"To examine the oligomeric state of sFKRP in solution, the solution structure of the sFKRP was analyzed by small-angle X-ray scattering with size exclusion chromatography (SEC-SAXS) (Fig. 2a, b).[...]The molecular weight was calculated as 214 kDa from the Porod volume of each P(r) function, suggesting that the sFKRP forms a tetramer in solution."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:9606(human-293s)|taxid:9606(Human 293S cell line)	-	2020/11/11	2020/11/11	rogid:s+HbseVnOLubWt0t2LFelTTGEvQ9606	rogid:s+HbseVnOLubWt0t2LFelTTGEvQ9606	rigid:iX7Kvig2hsKnYw6w684FHwM/CbM	false	sufficient binding region:45-495	sufficient binding region:45-495	4	0	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:Q9H9S5	uniprotkb:Q9H9S5	intact:EBI-21505709|ensembl:ENSP00000326570|ensembl:ENSP00000375776|uniprotkb:A8K5G7	intact:EBI-21505709|ensembl:ENSP00000326570|ensembl:ENSP00000375776|uniprotkb:A8K5G7	psi-mi:fkrp_human(display_long)|uniprotkb:Ribitol-5-phosphate transferase(gene name synonym)|uniprotkb:FKRP(gene name)|psi-mi:FKRP(display_short)	psi-mi:fkrp_human(display_long)|uniprotkb:Ribitol-5-phosphate transferase(gene name synonym)|uniprotkb:FKRP(gene name)|psi-mi:FKRP(display_short)	psi-mi:"MI:0071"(molecular sieving)	Kuwabara et al. (2020)	pubmed:31949166|imex:IM-28494	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-26444995|imex:IM-28494-5	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	ensembl:ENSG00000181027(gene)|ensembl:ENST00000318584(transcript)|ensembl:ENST00000391909(transcript)|go:"GO:0000139"(Golgi membrane)|go:"GO:0002162"(dystroglycan binding)|go:"GO:0005615"(extracellular space)|go:"GO:0005654"(nucleoplasm)|go:"GO:0005791"(rough endoplasmic reticulum)|go:"GO:0005794"(Golgi apparatus)|go:"GO:0005829"(cytosol)|go:"GO:0016021"(integral component of membrane)|go:"GO:0016485"(protein processing)|go:"GO:0016740"(transferase activity)|go:"GO:0035269"(protein O-linked mannosylation)|go:"GO:0042383"(sarcolemma)|go:"GO:0042802"(identical protein binding)|interpro:IPR007074(LicD protein)|mint:Q9H9S5|rcsb pdb:6KAJ|rcsb pdb:6KAK|rcsb pdb:6KAL|rcsb pdb:6KAM|rcsb pdb:6KAN|rcsb pdb:6L7S|rcsb pdb:6L7T|rcsb pdb:6L7U|refseq:NP_001034974.1|refseq:NP_077277.1|refseq:XP_005259304.1|refseq:XP_005259305.1|refseq:XP_005259306.1|refseq:XP_011525608.1|refseq:XP_011525609.1|refseq:XP_016882786.1	ensembl:ENSG00000181027(gene)|ensembl:ENST00000318584(transcript)|ensembl:ENST00000391909(transcript)|go:"GO:0000139"(Golgi membrane)|go:"GO:0002162"(dystroglycan binding)|go:"GO:0005615"(extracellular space)|go:"GO:0005654"(nucleoplasm)|go:"GO:0005791"(rough endoplasmic reticulum)|go:"GO:0005794"(Golgi apparatus)|go:"GO:0005829"(cytosol)|go:"GO:0016021"(integral component of membrane)|go:"GO:0016485"(protein processing)|go:"GO:0016740"(transferase activity)|go:"GO:0035269"(protein O-linked mannosylation)|go:"GO:0042383"(sarcolemma)|go:"GO:0042802"(identical protein binding)|interpro:IPR007074(LicD protein)|mint:Q9H9S5|rcsb pdb:6KAJ|rcsb pdb:6KAK|rcsb pdb:6KAL|rcsb pdb:6KAM|rcsb pdb:6KAN|rcsb pdb:6L7S|rcsb pdb:6L7T|rcsb pdb:6L7U|refseq:NP_001034974.1|refseq:NP_077277.1|refseq:XP_005259304.1|refseq:XP_005259305.1|refseq:XP_005259306.1|refseq:XP_011525608.1|refseq:XP_011525609.1|refseq:XP_016882786.1	-	-	-	figure legend:Fig. 2C|comment:"In the SEC analysis, the apparent molecular weight of the mutated proteins was lower than that of the WT, suggesting dissociation of a subunit(s) from the tetramer (Fig. 2c)."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:9606(human-293s)|taxid:9606(Human 293S cell line)	-	2020/11/11	2020/11/11	rogid:s+HbseVnOLubWt0t2LFelTTGEvQ9606	rogid:s+HbseVnOLubWt0t2LFelTTGEvQ9606	rigid:iX7Kvig2hsKnYw6w684FHwM/CbM	false	mutation disrupting interaction strength:88-88|mutation disrupting interaction strength:221-221|sufficient binding region:45-495|mutation disrupting interaction strength:276-276	mutation disrupting interaction strength:88-88|mutation disrupting interaction strength:221-221|sufficient binding region:45-495|mutation disrupting interaction strength:276-276	4	0	psi-mi:"MI:0113"(western blot)	psi-mi:"MI:0113"(western blot)